SODC_DROWI
ID SODC_DROWI Reviewed; 153 AA.
AC P41973; B4N5E2;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Superoxide dismutase [Cu-Zn] {ECO:0000250|UniProtKB:P61851};
DE EC=1.15.1.1;
DE AltName: Full=Superoxide dismutase 1 {ECO:0000250|UniProtKB:P61851};
GN Name=Sod1 {ECO:0000250|UniProtKB:P61851};
GN Synonyms=Sod {ECO:0000250|UniProtKB:P61851}; ORFNames=GK20556;
OS Drosophila willistoni (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7260;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7926818; DOI=10.1016/0378-1119(94)90085-x;
RA Kwiatowski J., Latorre A., Skarecky D., Ayala F.J.;
RT "Characterization of a Cu/Zn superoxide dismutase-encoding gene region in
RT Drosophila willistoni.";
RL Gene 147:295-296(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tucson 14030-0811.24;
RX PubMed=17994087; DOI=10.1038/nature06341;
RG Drosophila 12 genomes consortium;
RT "Evolution of genes and genomes on the Drosophila phylogeny.";
RL Nature 450:203-218(2007).
CC -!- FUNCTION: Destroys radicals which are normally produced within the
CC cells and which are toxic to biological systems.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 superoxide = H2O2 + O2; Xref=Rhea:RHEA:20696,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:18421; EC=1.15.1.1;
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 1 copper ion per subunit. {ECO:0000250};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the Cu-Zn superoxide dismutase family.
CC {ECO:0000305}.
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DR EMBL; L13281; AAA57250.1; -; Genomic_DNA.
DR EMBL; CH964101; EDW79581.1; -; Genomic_DNA.
DR RefSeq; XP_002068595.1; XM_002068559.2.
DR AlphaFoldDB; P41973; -.
DR SMR; P41973; -.
DR STRING; 7260.FBpp0249699; -.
DR EnsemblMetazoa; FBtr0251207; FBpp0249699; FBgn0013156.
DR GeneID; 6645808; -.
DR KEGG; dwi:6645808; -.
DR eggNOG; KOG0441; Eukaryota.
DR HOGENOM; CLU_056632_4_1_1; -.
DR InParanoid; P41973; -.
DR OMA; AQRGFHI; -.
DR OrthoDB; 1574423at2759; -.
DR PhylomeDB; P41973; -.
DR Proteomes; UP000007798; Unassembled WGS sequence.
DR GO; GO:0005777; C:peroxisome; IEA:EnsemblMetazoa.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:EnsemblMetazoa.
DR GO; GO:0004784; F:superoxide dismutase activity; IEA:UniProtKB-EC.
DR GO; GO:0001306; P:age-dependent response to oxidative stress; IEA:EnsemblMetazoa.
DR GO; GO:0008340; P:determination of adult lifespan; IEA:EnsemblMetazoa.
DR GO; GO:1903146; P:regulation of autophagy of mitochondrion; IEA:EnsemblMetazoa.
DR GO; GO:0048167; P:regulation of synaptic plasticity; IEA:EnsemblMetazoa.
DR GO; GO:2000331; P:regulation of terminal button organization; IEA:EnsemblMetazoa.
DR CDD; cd00305; Cu-Zn_Superoxide_Dismutase; 1.
DR Gene3D; 2.60.40.200; -; 1.
DR InterPro; IPR036423; SOD-like_Cu/Zn_dom_sf.
DR InterPro; IPR024134; SOD_Cu/Zn_/chaperone.
DR InterPro; IPR018152; SOD_Cu/Zn_BS.
DR InterPro; IPR001424; SOD_Cu_Zn_dom.
DR PANTHER; PTHR10003; PTHR10003; 1.
DR Pfam; PF00080; Sod_Cu; 1.
DR PRINTS; PR00068; CUZNDISMTASE.
DR SUPFAM; SSF49329; SSF49329; 1.
DR PROSITE; PS00087; SOD_CU_ZN_1; 1.
DR PROSITE; PS00332; SOD_CU_ZN_2; 1.
PE 3: Inferred from homology;
KW Antioxidant; Copper; Cytoplasm; Disulfide bond; Metal-binding;
KW Oxidoreductase; Reference proteome; Zinc.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..153
FT /note="Superoxide dismutase [Cu-Zn]"
FT /id="PRO_0000164099"
FT BINDING 45
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 47
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 70
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 82
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="structural"
FT /evidence="ECO:0000250"
FT BINDING 119
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT DISULFID 56..145
FT /evidence="ECO:0000250"
SQ SEQUENCE 153 AA; 15543 MW; 40F798E2285237CE CRC64;
MVVKAVCVIN GDAKGTVFFE QEDNGAPVKV TGEVTGLGKG LHGFHVHEFG DNTNGCMSSG
PHFNPHSKEH GAPGDENRHL GDLGNIEASG SGPTAVNITD SKITLVGANS IIGRTVVVHA
DPDDLGKGGH ELSKTTGNAG ARIGCGVIGI AKI
